Inhibition of degranulation of human polymorphonuclear leukocytes by complement factor D

FEBS Lett. 1995 Sep 11;371(3):300-2. doi: 10.1016/0014-5793(95)00926-z.

Abstract

A degranulation inhibiting protein could be isolated from human plasma ultrafiltrate by a three-step purification method including ion-exchange chromatography, gelfiltration and affinity-chromatography. The protein was identified as complement factor D by means of sequence analysis. Its degranulation inhibiting activity was determined with regard to its effect on the FNLPNTL-induced lactoferrin secretion of human polymorphonuclear leukocytes. Complement factor D caused a dose-dependent decrease of the FNLPNTL-stimulated lactoferrin degranulation down to 34% of stimulated controls.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Degranulation / physiology*
  • Complement Factor D / isolation & purification
  • Complement Factor D / physiology*
  • Humans
  • Molecular Sequence Data
  • Neutrophils / physiology*
  • Ultrafiltration

Substances

  • CFD protein, human
  • Complement Factor D